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dc.creatorOgnjenović, Jana
dc.creatorMilčić-Matić, Natalija
dc.creatorSmiljanić, Katarina
dc.creatorVucković, Olga
dc.creatorBurazer, Lidija
dc.creatorPopović, Nikola
dc.creatorStanić-Vučinić, Dragana
dc.creatorĆirković-Veličković, Tanja
dc.date.accessioned2020-06-03T13:41:27Z
dc.date.available2020-06-03T13:41:27Z
dc.date.issued2013
dc.identifier.issn0165-2427
dc.identifier.urihttp://vet-erinar.vet.bg.ac.rs/handle/123456789/998
dc.description.abstractCanine atopic dermatitis (CAD) is an immune system disorder that affects 10-15% of the canine population. Short ragweed (Ambrosia artemisiifolia) pollen represents one of the major seasonal sources of allergenic pollen proteins in Europe, particularly in the Pannonian valley of the Balkan region. In Serbia, about 66% of atopic dogs showed a positive intradermal skin test with its pollen extract, which is second to house dust mites. Therefore, characterization of Ambrosia artemisiifolia pollen components, in terms of defining major and minor allergens that induce clinically manifested allergic reaction in dogs, is important for valid diagnosis and efficient therapy. This study has, for the first time, characterized and identified major Ambrosia artemisiifolia allergens in CAD, using an immunoproteomic approach. To assess the prevalence of specific IgE in electrophoretically separated ragweed pollen proteins, individual reactivity of sera from dogs with CAD was analyzed and compared to the reactivity of sera from healthy dogs in the non-reducing conditions, which were found optimal for specific canine IgE detection. A specific IgE band (38 kDa) was recognized as the most dominant allergen in CAD, occurring in 81% of positive dogs sera. 2-D immunoblotting followed by a mass spectrometry peptide fingerprint analyses with pooled canine and human atopic sera, revealed that 38 kDa major Ambrosia atremisiifolia allergens in CAD were all five isoallergens of the Amb a 1 group (antigen E), including the previously named Amb a 2 (antigen K). In contrast to canine sera, human atopic sera also recognized lower mass allergens such as the 13 fragment of Amb a 1 and profilins (Amb a 8 variants). The most prominent ragweed proteins in CAD, represent, as in humans, variants of all five isoallergens of the Amb a 1 group (pectate lyase): Amb a 1.0101 and its natural variant E1XUL2, Amb a 1.0202, 1.0304, 1.0402 and the natural variant of Amb a 1.0501, E1XUM0, as well as the a fragment of pollen allergen Amb a 1.0201.en
dc.publisherElsevier Science Bv, Amsterdam
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.rightsrestrictedAccess
dc.sourceVeterinary Immunology and Immunopathology
dc.subjectAmb a 1 allergensen
dc.subjectAmbrosia artemisiifolia pollenen
dc.subjectCanine atopic dermatitisen
dc.subjectDogen
dc.subjectImmunoproteomicsen
dc.subjectShort ragweeden
dc.titleImmunoproteomic characterization of Ambrosia artemisiifolia pollen allergens in canine atopic dermatitisen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractЋирковић-Величковић, Тања; Станић-Вучинић, Драгана; Огњеновић, Јана; Смиљанић, Катарина; Поповић, Никола; Вуцковић, Олга; Милчић-Матић, Наталија; Буразер, Лидија;
dc.citation.volume155
dc.citation.issue1-2
dc.citation.spage38
dc.citation.epage47
dc.citation.other155(1-2): 38-47
dc.citation.rankM21
dc.identifier.wos000323457700005
dc.identifier.doi10.1016/j.vetimm.2013.06.005
dc.identifier.pmid23830203
dc.identifier.scopus2-s2.0-84881024086
dc.identifier.rcubconv_1932
dc.type.versionpublishedVersion


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